A light scattering photometer has been built to permit the observation of hemoglobin S aggregation at 1.06 micron. The light scattering properties of concentrated hemoglobin deoxyhemoglobin S solutions have been examined as a function of time after temperature jumps. The scattered intensity can be followed over changes in signal which span over four decades in sensitivity. More complete studies of the light scattering appear warranted and will be pursued to provide information on the mechanism which controls the rate of polymerization. Computer simulations of mechanisms will also be implemented in order to theoretically explore the dynamics of polymer formation. Simple equilibrium and steady-state nucleation models have been shown to provide an adequate description of the concentration, temperature, and solubility dependence of the observed rates, and to rationalize the slowness of the rates observed under the conditions of our experiments.